HIS8_ARATH
ID HIS8_ARATH Reviewed; 466 AA.
AC Q9C5U8; F4KC60; Q8LA77; Q9FN00;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Histidinol dehydrogenase, chloroplastic;
DE Short=HDH;
DE EC=1.1.1.23;
DE AltName: Full=Protein HISTIDINE BIOSYNTHESIS 8;
DE Flags: Precursor;
GN Name=HISN8; Synonyms=HDH; OrderedLocusNames=At5g63890; ORFNames=MGI19.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Fujimori K.;
RT "Isolation of Arabidopsis cDNA for histidinol dehydrogenase.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547652; DOI=10.1007/s00726-005-0247-0;
RA Stepansky A., Leustek T.;
RT "Histidine biosynthesis in plants.";
RL Amino Acids 30:127-142(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17434988; DOI=10.1104/pp.107.096511;
RA Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.;
RT "Genetic dissection of histidine biosynthesis in Arabidopsis.";
RL Plant Physiol. 144:890-903(2007).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC ChEBI:CHEBI:57945; EC=1.1.1.23;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5U8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5U8-2; Sequence=VSP_047341;
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB027709; BAB40445.1; -; mRNA.
DR EMBL; AB007646; BAB11037.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97811.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97812.1; -; Genomic_DNA.
DR EMBL; AY039881; AAK63985.1; -; mRNA.
DR EMBL; AY143900; AAN28839.1; -; mRNA.
DR EMBL; AY087987; AAM65533.1; -; mRNA.
DR RefSeq; NP_568981.2; NM_125784.3. [Q9C5U8-1]
DR RefSeq; NP_851260.1; NM_180929.4. [Q9C5U8-2]
DR AlphaFoldDB; Q9C5U8; -.
DR SMR; Q9C5U8; -.
DR BioGRID; 21751; 3.
DR STRING; 3702.AT5G63890.2; -.
DR iPTMnet; Q9C5U8; -.
DR PaxDb; Q9C5U8; -.
DR PRIDE; Q9C5U8; -.
DR ProteomicsDB; 230200; -. [Q9C5U8-1]
DR EnsemblPlants; AT5G63890.1; AT5G63890.1; AT5G63890. [Q9C5U8-2]
DR EnsemblPlants; AT5G63890.2; AT5G63890.2; AT5G63890. [Q9C5U8-1]
DR GeneID; 836509; -.
DR Gramene; AT5G63890.1; AT5G63890.1; AT5G63890. [Q9C5U8-2]
DR Gramene; AT5G63890.2; AT5G63890.2; AT5G63890. [Q9C5U8-1]
DR KEGG; ath:AT5G63890; -.
DR Araport; AT5G63890; -.
DR TAIR; locus:2163946; AT5G63890.
DR eggNOG; KOG2697; Eukaryota.
DR InParanoid; Q9C5U8; -.
DR OMA; MVTGPGN; -.
DR PhylomeDB; Q9C5U8; -.
DR UniPathway; UPA00031; UER00014.
DR PRO; PR:Q9C5U8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5U8; baseline and differential.
DR Genevisible; Q9C5U8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009411; P:response to UV; IEP:TAIR.
DR CDD; cd06572; Histidinol_dh; 1.
DR HAMAP; MF_01024; HisD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR001692; Histidinol_DH_CS.
DR InterPro; IPR022695; Histidinol_DH_monofunct.
DR InterPro; IPR012131; Hstdl_DH.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PIRSF; PIRSF000099; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Amino-acid biosynthesis; Chloroplast;
KW Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 31..466
FT /note="Histidinol dehydrogenase, chloroplastic"
FT /id="PRO_0000007215"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..25
FT /note="MSLNLSRLSLLSSPRISISTHAPRK -> MNEFVDQLRFT (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_047341"
FT CONFLICT 25
FT /note="K -> KA (in Ref. 2; BAB11037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 50323 MW; 1175DEA979244595 CRC64;
MSLNLSRLSL LSSPRISIST HAPRKGYVCC SMKSYRLSEL SSSQVDSLKS RPRIDFSSIF
ATVNPIIDAV RSNGDNAVKE YTERFDKVQL NKVVEDMSEL SVPELDSNVK EAFDVAYDNI
YAFHLAQKST EKSVENMKGV RCKRVSRSIG SVGLYVPGGT AVLPSTALML AIPAQIAGCK
TVVLATPPSK DGSICKEVLY CAKRAGVTHI LKAGGAQAIA AMAWGTDSCP KVEKIFGPGN
QYVTAAKMIL QNSEAMVSID MPAGPSEVLV IADEHASPVY IAADLLSQAE HGPDSQVVLV
VVGDSVDLNA IEEEIAKQCK SLPRGEFASK ALSHSFTVFA RDMIEAISFS NLYAPEHLII
NVKDAEKWEG LIENAGSVFI GPWTPESVGD YASGTNHVLP TYGYARMYSG VSLDSFLKFM
TVQSLTEEGL RNLGPYVATM AEIEGLDAHK RAVTLRLKDI EAKQLA
